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D5EQ72 (D5EQ72_CORAD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase HAMAP-Rule MF_00687
EC=5.3.1.17 HAMAP-Rule MF_00687
Alternative name(s):
5-keto-4-deoxyuronate isomerase HAMAP-Rule MF_00687
DKI isomerase HAMAP-Rule MF_00687
Gene names
Name:kduI HAMAP-Rule MF_00687
Ordered Locus Names:Caka_0816
OrganismCoraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865) [Complete proteome] [HAMAP]
Taxonomic identifier583355 [NCBI]
Taxonomic lineageBacteria › Verrucomicrobia › Opitutae › Puniceicoccales › Puniceicoccaceae › Coraliomargarita ›

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate By similarity. HAMAP-Rule MF_00687 SAAS SAAS021120

Catalytic activity

5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-hexodiulosonate. HAMAP-Rule MF_00687 SAAS SAAS021120

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00687 SAAS SAAS021120

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 4/5. HAMAP-Rule MF_00687 SAAS SAAS021120

Sequence similarities

Belongs to the KduI family. HAMAP-Rule MF_00687

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding1941Zinc By similarity HAMAP-Rule MF_00687
Metal binding1961Zinc By similarity HAMAP-Rule MF_00687
Metal binding2011Zinc By similarity HAMAP-Rule MF_00687
Metal binding2431Zinc By similarity HAMAP-Rule MF_00687

Sequences

Sequence LengthMass (Da)Tools
D5EQ72 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 5276FF77617822D5

FASTA27630,679
        10         20         30         40         50         60 
MESRYATGIN EYKSMNTAQL RDAFLIDQLF KEDEVHLQYC ETDRTIVGSA VPTSTELALE 

        70         80         90        100        110        120 
AGSALAAEYF CERRELGILN LGASGTVQVD GETYTLDTLD CLYVGRGSRD IRFISASADQ 

       130        140        150        160        170        180 
PAQFYLASYP AHTSYPTTLT KRSAANPIQL GDTHNANKRT IYQYIHEGGV QSCQLVMGIT 

       190        200        210        220        230        240 
ALEDGSVWNT MPAHTHERRT EVYLYFNVDE DATVFHFMGT GDETRHITVH DKQAVISPAW 

       250        260        270 
SIHSGSGTRN YSFAWCMGGE NQDFSDMQGI PIQALK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001998 Genomic DNA. Translation: ADE53840.1.
RefSeqYP_003548010.1. NC_014008.1.

3D structure databases

ProteinModelPortalD5EQ72.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE53840; ADE53840; Caka_0816.
GeneID8957936.
KEGGcaa:Caka_0816.
PATRIC35442220. VBICorAka2911_0794.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000124379.
KOK01815.
OMALDCLYVG.

Enzyme and pathway databases

BioCycCAKA583355:GI4D-823-MONOMER.
UniPathwayUPA00545; UER00826.

Family and domain databases

HAMAPMF_00687. KduI.
InterProIPR007045. KduI.
IPR021120. KduI/IolB_isomerase.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF04962. KduI. 1 hit.
[Graphical view]
PIRSFPIRSF006625. KduI. 1 hit.
SUPFAMSSF51182. RmlC_like_cupin. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD5EQ72_CORAD
AccessionPrimary (citable) accession number: D5EQ72
Entry history
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info